BMRB Entry 30037
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30037
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Title: NMR Structure of NS5A-D2 (JFH1) peptide (304-323) PubMed: 31315928
Deposition date: 2016-03-18 Original release date: 2019-07-15
Authors: Dujardin, M.; Cantrelle, F.; Lippens, G.; Hanoulle, X.
Citation: Dujardin, Marie; Madan, Vanesa; Gandhi, Neha; Cantrelle, Francois-Xavier; Launay, Helene; Huvent, Isabelle; Bartenschlager, Ralf; Lippens, Guy; Hanoulle, Xavier. "Cyclophilin A allows the allosteric regulation of a structural motif in the disordered domain 2 of NS5A and thereby fine-tunes HCV RNA replication" J. Biol Chem. 294, 13171-13185 (2019).
Assembly members:
entity_1, polymer, 20 residues, 2268.570 Da.
Natural source: Common Name: HCV Taxonomy ID: 356411 Superkingdom: Viruses Kingdom: not available Genus/species: Hepacivirus 'Hepatitis C virus
Experimental source: Production method: recombinant technology Host organism: Escherchia coli BL21(DE3) Vector: pET32a
Entity Sequences (FASTA):
entity_1: GFPRALPAWARPDYNPPLVE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 66 |
| 15N chemical shifts | 20 |
| 1H chemical shifts | 138 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 20 residues - 2268.570 Da.
| 1 | GLY | PHE | PRO | ARG | ALA | LEU | PRO | ALA | TRP | ALA | |
| 2 | ARG | PRO | ASP | TYR | ASN | PRO | PRO | LEU | VAL | GLU |
Samples:
sample_1: NS5A-D2(JFH1)peptide 304-323, unlabelled, 5 mM; NaCl 30 mM
sample_2: 15N 13C NS5A-D2(JFH1)peptide 304-323, [U-99% 13C; U-99% 15N], 1 mM; NaCl 30 mM
sample_conditions_1: ionic strength: 30 mM; pH: 6.4; pressure: 1 bar; temperature: 298 K
sample_conditions_2: ionic strength: 30 mM; pH: 6.4; pressure: 1 bar; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N_HSQC | sample_1 | isotropic | sample_conditions_1 |
| HNCACB | sample_2 | isotropic | sample_conditions_2 |
| HNCOACB | sample_2 | isotropic | sample_conditions_2 |
| HNCO | sample_2 | isotropic | sample_conditions_2 |
| HNCACO | sample_2 | isotropic | sample_conditions_2 |
| 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N_HSQC | sample_2 | isotropic | sample_conditions_2 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts